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Volumn 4, Issue 3, 2005, Pages 950-957

Tagging-via-substrate strategy for probing O-GlcNAc modified proteins

Author keywords

Glycosylation; O GlcNAc; Post translational modifications; Proteomics; Staudinger ligation; Tagging via substrate

Indexed keywords

N ACETYLGLUCOSAMINE;

EID: 20844457419     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr050033j     Document Type: Article
Times cited : (115)

References (37)
  • 1
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • Torres, C. R.; Hart, G. W. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J. Biol. Chem. 1984, 259, 3308-3317.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 2
    • 0036462599 scopus 로고    scopus 로고
    • The emerging significance of O-GlcNAc in cellular regulation
    • Zachara, N. E.; Hart, G. W. The emerging significance of O-GlcNAc in cellular regulation. Chem. Rev. 2002, 102, 431-438.
    • (2002) Chem. Rev. , vol.102 , pp. 431-438
    • Zachara, N.E.1    Hart, G.W.2
  • 3
    • 3042613480 scopus 로고    scopus 로고
    • O-GlcNAc a sensor of cellular state: The role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress
    • Zachara, N. E.; Hart, G. W. O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress. Biochim. Biophys. Acta 2004, 1673, 13-28.
    • (2004) Biochim. Biophys. Acta , vol.1673 , pp. 13-28
    • Zachara, N.E.1    Hart, G.W.2
  • 4
    • 0036898933 scopus 로고    scopus 로고
    • Diverse regulation of protein function by O-GlcNAc: A nuclear and cytoplasmic carbohydrate posttranslational modification
    • Vosseller, K.; Sakabe, K.; Wells, L.; Hart, G. W. Diverse regulation of protein function by O-GlcNAc: a nuclear and cytoplasmic carbohydrate posttranslational modification. Curr. Opin. Chem. Biol. 2002, 6, 851-857.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 851-857
    • Vosseller, K.1    Sakabe, K.2    Wells, L.3    Hart, G.W.4
  • 5
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc
    • Wells, L.; Vosseller, K.; Hart, G. W. Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 2001, 291, 2376-2378.
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 6
    • 0034854157 scopus 로고    scopus 로고
    • Glycan-dependent signaling: O-linked N-acetylglucosamine
    • Hanover, J. A. Glycan-dependent signaling: O-linked N-acetylglucosamine. Faseb J. 2001, 15, 1865-1876.
    • (2001) Faseb J. , vol.15 , pp. 1865-1876
    • Hanover, J.A.1
  • 7
    • 0026795976 scopus 로고
    • Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine: Polypeptide beta-N-acetylglucosaminyltransferase
    • Haltiwanger, R. S.; Blomberg, M. A.; Hart, G. W. Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine: polypeptide beta-N-acetylglucosaminyltransferase. J. Biol. Chem. 1992, 267, 9005-9013.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9005-9013
    • Haltiwanger, R.S.1    Blomberg, M.A.2    Hart, G.W.3
  • 8
    • 0028085881 scopus 로고
    • Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol
    • Dong, D. L.; Hart, G. W. Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol. J. Biol. Chem. 1994, 269, 19321-19330.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19321-19330
    • Dong, D.L.1    Hart, G.W.2
  • 9
    • 0842347416 scopus 로고    scopus 로고
    • Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability
    • O'Donnell, N.; Zachara, N. E.; Hart, G. W.; Marth, J. D. Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability. Mol. Cell Biol. 2004, 24, 1680-1690.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 1680-1690
    • O'Donnell, N.1    Zachara, N.E.2    Hart, G.W.3    Marth, J.D.4
  • 10
    • 0037300799 scopus 로고    scopus 로고
    • A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance
    • Wells, L.; Vosseller, K.; Hart, G. W. A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance. Cell Mol. Life Sci. 2003, 60, 222-228.
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 222-228
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 11
    • 0037117511 scopus 로고    scopus 로고
    • Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes
    • Vosseller, K.; Wells, L.; Lane, M. D.; Hart, G. W. Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 5313-5318.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5313-5318
    • Vosseller, K.1    Wells, L.2    Lane, M.D.3    Hart, G.W.4
  • 12
    • 0036679303 scopus 로고    scopus 로고
    • Altered glycan-dependent signaling induces insulin resistance and hyperleptinemia
    • McClain, D. A. et al. Altered glycan-dependent signaling induces insulin resistance and hyperleptinemia. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 10695-10699.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10695-10699
    • McClain, D.A.1
  • 14
    • 0034677879 scopus 로고    scopus 로고
    • Cell surface engineering by a modified Staudinger reaction
    • Saxon, E.; Bertozzi, C. R. Cell surface engineering by a modified Staudinger reaction. Science 2000, 287, 2007-2010.
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 16
    • 4344704630 scopus 로고    scopus 로고
    • Chemical remodelling of cell surfaces in living animals
    • Prescher, J. A.; Dube, D. H.; Bertozzi, C. R. Chemical remodelling of cell surfaces in living animals. Nature 2004, 430, 873-877.
    • (2004) Nature , vol.430 , pp. 873-877
    • Prescher, J.A.1    Dube, D.H.2    Bertozzi, C.R.3
  • 17
    • 4344584507 scopus 로고    scopus 로고
    • A tagging-via-substrate technology for detection and proteomics of farnesylated proteins
    • Kho, Y. et al. A tagging-via-substrate technology for detection and proteomics of farnesylated proteins. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 12479-12484.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12479-12484
    • Kho, Y.1
  • 18
    • 0037132659 scopus 로고    scopus 로고
    • Investigating cellular metabolism of synthetic azidosugars with the Staudinger ligation
    • Saxon, E. et al. Investigating cellular metabolism of synthetic azidosugars with the Staudinger ligation. J. Am. Chem. Soc. 2002, 124, 14893-14902.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14893-14902
    • Saxon, E.1
  • 19
    • 4544310350 scopus 로고    scopus 로고
    • Expanding the diversity of unnatural cell-surface sialic acids
    • Luchansky, S. J.; Goon, S.; Bertozzi, C. R. Expanding the diversity of unnatural cell-surface sialic acids. Chembiochem 2004, 5, 371-374.
    • (2004) Chembiochem , vol.5 , pp. 371-374
    • Luchansky, S.J.1    Goon, S.2    Bertozzi, C.R.3
  • 20
    • 0035179085 scopus 로고    scopus 로고
    • Chemical and biological strategies for engineering cell surface glycosylation
    • Saxon, E.; Bertozzi, C. R. Chemical and biological strategies for engineering cell surface glycosylation. Annu. Rev. Cell Dev. Biol. 2001, 17, 1-23.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 1-23
    • Saxon, E.1    Bertozzi, C.R.2
  • 21
    • 2442703973 scopus 로고    scopus 로고
    • Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins
    • Zhao, Y.; Kwon, S. W.; Anselmo, A.; Kaur, K.; White, M. A. Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins. J. Biol. Chem. 2004, 279, 20999-21002.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20999-21002
    • Zhao, Y.1    Kwon, S.W.2    Anselmo, A.3    Kaur, K.4    White, M.A.5
  • 22
    • 20844451833 scopus 로고    scopus 로고
    • Selective enrichment of thiophosphorylated polypeptides as a tool for the analysis of protein phosphorylation
    • Kwon, S. W.; Kim, S. C.; Jaunbergs, J.; Falck, J. R.; Zhao, Y. Selective enrichment of thiophosphorylated polypeptides as a tool for the analysis of protein phosphorylation. Mol. Cell Proteomics 2003, 2, 242-247.
    • (2003) Mol. Cell Proteomics , vol.2 , pp. 242-247
    • Kwon, S.W.1    Kim, S.C.2    Jaunbergs, J.3    Falck, J.R.4    Zhao, Y.5
  • 23
    • 0037304213 scopus 로고    scopus 로고
    • High glucose and insulin promote O-GlcNAc modification of proteins, including alpha-tubulin
    • Walgren, J. L.; Vincent, T. S.; Schey, K. L.; Buse, M. G. High glucose and insulin promote O-GlcNAc modification of proteins, including alpha-tubulin. Am. J. Physiol. Endocrinol. Metab. 2003, 284, E424-434.
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.284
    • Walgren, J.L.1    Vincent, T.S.2    Schey, K.L.3    Buse, M.G.4
  • 24
    • 0034614349 scopus 로고    scopus 로고
    • Glucose and streptozotocin stimulate p135 O-glycosylation in pancreatic islets
    • Konrad, R. J.; Janowski, K. M.; Kudlow, J. E. Glucose and streptozotocin stimulate p135 O-glycosylation in pancreatic islets. Biochem. Biophys. Res. Commun. 2000, 267, 26-32.
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 26-32
    • Konrad, R.J.1    Janowski, K.M.2    Kudlow, J.E.3
  • 25
    • 0034663705 scopus 로고    scopus 로고
    • Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration
    • Han, I.; Oh, E. S.; Kudlow, J. E. Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration. Biochem. J. 2000, 350 Pt 1, 109-114.
    • (2000) Biochem. J. , vol.350 , Issue.PART 1 , pp. 109-114
    • Han, I.1    Oh, E.S.2    Kudlow, J.E.3
  • 26
    • 0031943723 scopus 로고    scopus 로고
    • Insulin and glucosamine infusions increase O-linked N-acetyl-glucosamine in skeletal muscle proteins in vivo
    • Yki-Jarvinen, H.; Virkamaki, A.; Daniels, M. C.; McClain, D.; Gottschalk, W. K. Insulin and glucosamine infusions increase O-linked N-acetyl-glucosamine in skeletal muscle proteins in vivo. Metabolism 1998, 47, 449-555.
    • (1998) Metabolism , vol.47 , pp. 449-555
    • Yki-Jarvinen, H.1    Virkamaki, A.2    Daniels, M.C.3    McClain, D.4    Gottschalk, W.K.5
  • 27
    • 0030926433 scopus 로고    scopus 로고
    • Role of the glucosamine pathway in fat-induced insulin resistance
    • Hawkins, M. et al. Role of the glucosamine pathway in fat-induced insulin resistance. J. Clin. Invest. 1997, 99, 2173-2182.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2173-2182
    • Hawkins, M.1
  • 28
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki, K.; Zhu, T.; Guan, K. L. TSC2 mediates cellular energy response to control cell growth and survival. Cell 2003, 115, 577-590.
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 29
    • 3042534011 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells
    • Zachara, N. E. et al. Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells. J. Biol. Chem. 2004, 279, 30133-30142.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30133-30142
    • Zachara, N.E.1
  • 30
    • 0035876021 scopus 로고    scopus 로고
    • Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine
    • Comer, F. I.; Vosseller, K.; Wells, L.; Accavitti, M. A.; Hart, G. W. Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine. Anal. Biochem. 2001, 293, 169-177.
    • (2001) Anal. Biochem. , vol.293 , pp. 169-177
    • Comer, F.I.1    Vosseller, K.2    Wells, L.3    Accavitti, M.A.4    Hart, G.W.5
  • 31
    • 0001028995 scopus 로고
    • Chaplin, M. F., Kennedy, J. F., Eds.; IRL Press: New York
    • Montreuil, J.; et al., in Carbohydrate Analysis: A Practical Approach; Chaplin, M. F., Kennedy, J. F., Eds.; IRL Press: New York, 1994, 181-293.
    • (1994) Carbohydrate Analysis: a Practical Approach , pp. 181-293
    • Montreuil, J.1
  • 32
    • 13844313887 scopus 로고    scopus 로고
    • Quantitative analysis of both protein expression and serine/threonine post-translational modifications through stable isotope labeling with dithiothreitol
    • Vosseller, K. et al. Quantitative analysis of both protein expression and serine/threonine post-translational modifications through stable isotope labeling with dithiothreitol. Proteomics 2005, 5, 388-398.
    • (2005) Proteomics , vol.5 , pp. 388-398
    • Vosseller, K.1
  • 33
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine posttranslational modifications
    • Wells, L. et al. Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine posttranslational modifications. Mol. Cell Proteomics 2002, 1, 791-804.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 791-804
    • Wells, L.1
  • 35
    • 0348014634 scopus 로고    scopus 로고
    • Improved beta-elimination-based affinity purification strategy for enrichment of phosphopeptides
    • McLachlin, D. T.; Chait, B. T. Improved beta-elimination-based affinity purification strategy for enrichment of phosphopeptides. Anal. Chem. 2003, 75, 6826-6836.
    • (2003) Anal. Chem. , vol.75 , pp. 6826-6836
    • McLachlin, D.T.1    Chait, B.T.2
  • 36
    • 4444337997 scopus 로고    scopus 로고
    • Exploring the O-GlcNAc proteome: Direct identification of O-GlcNAc-modified proteins from the brain
    • Khidekel, N.; Ficarro, S. B.; Peters, E. C.; Hsieh-Wilson, L. C. Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 13132-13137.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13132-13137
    • Khidekel, N.1    Ficarro, S.B.2    Peters, E.C.3    Hsieh-Wilson, L.C.4
  • 37
    • 15944377809 scopus 로고    scopus 로고
    • Quantitative Phosphoproteomics Applied to the Yeast Pheromone Signaling Pathway
    • Gruhler, A. et al. Quantitative Phosphoproteomics Applied to the Yeast Pheromone Signaling Pathway. Mol. Cell Proteomics 2005, 4, 310-327.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 310-327
    • Gruhler, A.1


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